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. 2012 Mar;194(6):1447–1456. doi: 10.1128/JB.06590-11

Table 2.

Kinetic constants of HDH and group X ALDHa

Enzyme Strain Km (μM) for:
kcat (min−1) for:
kcat/Km (min−1 μM−1) for:
VEH Acetaldehyde NAD+ NADP+ VEH Acetaldehyde VEH Acetaldehyde
HdhA P. aeruginosa 8.5 ± 2.2 19 ± 3 210 ± 40 1,700 ± 270 880 ± 80 980 ± 40 104 51.7
rHdhA P. aeruginosa 52 ± 19 15 ± 3 18 ± 1 670 ± 140 1,500 ± 300 1,510 ± 100 29 104
rHdhB P. aeruginosa 13 ± 2 15 ± 4 48 ± 8 640 ± 100 1,100 ± 100 1,100 ± 100 88 75
rOaHdh O. anthropi 16 ± 5 2.7 ± 0.7 124 ± 41 NA 60 ± 4 54 ± 2 3.7 8.9
rPdHdh P. denitrificans 65 ± 13 18 ± 6 900 ± 180 NA 91 ± 5 97 ± 7 1.4 5.3
rAldB E. coli 69 ± 15 2.8 ± 0.6 NA 170 ± 20 170 ± 10 160 ± 10 2.5 57
cHdhb C. palmioleophila 19.5 ± 3.6 14.3 ± 4 195 ± 23c 697 ± 79c 1,260 ± 66 1,180 ± 105 64.4 82.6
a

Enzyme activities were measured at fixed concentrations of either 1 mM NAD(P)+ or 1 mM VEH. Data are the means of four experiments (and the standard deviations for Km and kcat values). NA, not applicable due to low activity.

b

Data from Ito et al. (3).

c

Data obtained from double reciprocal plots.